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Protein–protein interaction networks are the networks of protein complexes formed by biochemical events and/or electrostatic forces and that serve a distinct biological function as a complex. The protein interactome describes the full repertoire of a biological system’s protein–protein interactions (PPIs).
The specific recognition of a proline-rich motif in the intrinsically disordered region of SF1 by the PRPF40A tandem WW domains is modulated by an intramolecular autoinhibition, suggesting a general mechanism to enhance WW binding selectivity.
Choosing best chemical cross-linking (XL) reagents and conditions for studying protein-protein interactions in structural biology is laborious and lacks in accuracy. The authors develop here an accurate, fast, robust and quantiative denaturing mass photometry approach for screening of XL conditions.
The combination of mass spectroscopy-based proteomics with molecular dynamics enables the in-depth study of metallothioneine-Zn(II) binding mechanisms, critical to cell homeostasis and Zn(II) ion buffering.
Co-fractionation mass spectrometry (CF-MS) has the potential to measure thousands of protein complexes in a single experiment, but the field is still in its infancy. A meta-analysis of CF-MS data yields a core CF-MS interactome and a tool allowing researchers to align new results to published data.